*HEADER    MEMBRANE PROTEIN                        22-MAY-06   2H3O              
*TITLE     STRUCTURE OF MERFT, A MEMBRANE PROTEIN WITH TWO TRANS-                
*TITLE    2 MEMBRANE HELICES                                                     
*COMPND    MOL_ID: 1;                                                            
*COMPND   2 MOLECULE: MERF;                                                      
*COMPND   3 CHAIN: A;                                                            
*COMPND   4 FRAGMENT: HELIX-LOOP-HELIX, RESIDUES 12-72;                          
*COMPND   5 ENGINEERED: YES;                                                     
*COMPND   6 MUTATION: YES                                                        
*SOURCE    MOL_ID: 1;                                                            
*SOURCE   2 ORGANISM_SCIENTIFIC: MORGANELLA MORGANII;                            
*SOURCE   3 ORGANISM_COMMON: BACTERIA;                                           
*SOURCE   4 GENE: MERF;                                                          
*SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
*SOURCE   6 EXPRESSION_SYSTEM_COMMON: BACTERIA;                                  
*SOURCE   7 EXPRESSION_SYSTEM_STRAIN: C43(DE3);                                  
*SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
*SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PET31B/MERFT                              
*KEYWDS    MEMBRANE PROTEIN, ALPHA-HELIX, BICELLE                                
*EXPDTA    NMR                                                                   
*AUTHOR    S.J.OPELLA, A.A.DE ANGELIS, S.C.HOWELL, A.A.NEVZOROV                  
*REVDAT   1   03-OCT-06 2H3O    0                                                
Residue	  15N Chemical Shift (ppm)	1H-15N Dipolar Coupling (Hz)
I13		137.5			1428
G14		123.3			962
T15		129.6			1286
T16		135.6			1609
L17		135.5			1367
V18		137.5			1428
A19		138.7			1479
L20		133.6			1483
S21		129			1198
S22		125.4			1183
F23		122.7			994
T24		104.7			690
P25		110			0
V26		86.5			1890
L27		84.9			3312
V28		93.4			3638
I29		93.5			2858
L30		84.7			2903
L31		86.3			3754
G32		88			3168
V33		94.1			2420
V34		85.9			3132
G35		88.1			3621
L36		94.4			3206
S37		86.3			2849
A38		81.8			3557
L39		94.2			3853
T40		95.2			2709
G41		79.8			2556
Y42		132.4			1161
L43		119.2			367
D44		107.9			659
Y45		124.7			1239
V46		100.5			793
L47		84.3			3344
L48		109.4			1537
P49a		110			0
A50		113.1			852
L51		99.8			2948
A52		98			2901
I53		82.4			2457
F54		86.3			3754
I55		100.6			3395
G56		79.8			2556
L57		80.5			2920
T58		89.1			3946
I59		98.7			3146
Y60		84.5			2672
A61		80			3290
I62		94.2			3853
Q63		98.4			2540
R64		79.7			2735
K65		86.3			3893
R66		94.4			3206
Q67		97.6			2477
A68		80			3290
D69		114.5			1025
A70		123.9			380
  Entry H atom name         Submitted Coord H atom name
    1    H    LEU  27           HN       LEU  27   0.029  -2.542  -0.129
    2    H    VAL  28           HN       VAL  28   1.954  -3.146   0.944
    3    H    ILE  29           HN       ILE  29   2.847  -1.169   2.223
    4    H    LEU  30           HN       LEU  30   1.028  -0.381   4.306
    5    H    LEU  31           HN       LEU  31   1.511  -2.844   5.869
    6    H    GLY  32           HN       GLY  32   4.005  -2.391   6.422
    7    H    VAL  33           HN       VAL  33   4.151  -0.045   7.660
    8    H    VAL  34           HN       VAL  34   2.703  -0.747   9.439
    9    H    GLY  35           HN       GLY  35   3.756  -2.374  10.561
   10    H    LEU  36           HN       LEU  36   5.942  -1.898  11.442
   11    H    SER  37           HN       SER  37   5.255  -0.055  13.237
   12    H    ALA  38           HN       ALA  38   4.534  -1.779  15.165
   13    H    LEU  39           HN       LEU  39   6.517  -2.874  16.114
   14    H    THR  40           HN       THR  40   7.835  -0.930  17.323
   15    H    GLY  41           HN       GLY  41   6.241  -0.391  18.803
   16    H    TYR  42           HN       TYR  42   5.985  -1.978  20.109
   17    H    LEU  43           HN       LEU  43   6.873  -3.124  20.908
   18    H    ASP  44           HN       ASP  44   7.334  -2.240  22.448
   19    H    TYR  45           HN       TYR  45   9.992  -2.589  22.058
   20    H    VAL  46           HN       VAL  46  14.495  -2.179  21.854
   21    H    LEU  47           HN       LEU  47  15.292  -3.518  20.098
   22    H    LEU  48           HN       LEU  48  13.248  -5.857  17.321
   23    H    ALA  50           HN       ALA  50  13.152 -10.771  18.393
   24    H    LEU  51           HN       LEU  51  11.327 -10.284  18.008
   25    H    ALA  52           HN       ALA  52  11.932  -8.219  17.100
   26    H    ILE  53           HN       ILE  53  13.807  -8.826  14.932
   27    H    PHE  54           HN       PHE  54  11.618  -9.733  13.297
   28    H    ILE  55           HN       ILE  55  10.381  -7.487  12.691
   29    H    GLY  56           HN       GLY  56  12.196  -5.981  11.596
   30    H    LEU  57           HN       LEU  57  13.295  -7.516   9.608
   31    H    THR  58           HN       THR  58  10.961  -8.103   8.358
   32    H    ILE  59           HN       ILE  59  10.268  -5.596   7.586
   33    H    TYR  60           HN       TYR  60  12.277  -4.591   5.733
   34    H    ALA  61           HN       ALA  61  11.310  -6.418   3.720
   35    H    ILE  62           HN       ILE  62   9.079  -5.157   2.841
   36    H    GLN  63           HN       GLN  63  10.046  -2.994   1.775
   37    H    ARG  64           HN       ARG  64  11.945  -3.586  -0.212
   38    H    LYS  65           HN       LYS  65   9.981  -4.869  -1.783
   39    H    ARG  66           HN       ARG  66   8.964  -2.598  -2.965
   40    H    GLN  67           HN       GLN  67  10.686  -1.785  -4.220
   41    H    ALA  68           HN       ALA  68  12.066  -3.419  -5.977
   42    H    ASP  69           HN       ASP  69   9.958  -2.836  -7.450
   43    H    ALA  70           HN       ALA  70   6.114  -3.155  -9.633